6d0a: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='6d0a' size='340' side='right'caption='[[6d0a]], [[Resolution|resolution]] 1.47Å' scene=''> | <StructureSection load='6d0a' size='340' side='right'caption='[[6d0a]], [[Resolution|resolution]] 1.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6d0a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D0A OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6d0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D0A FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4680942Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d0a OCA], [https://pdbe.org/6d0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d0a RCSB], [https://www.ebi.ac.uk/pdbsum/6d0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d0a ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/AADAT_HUMAN AADAT_HUMAN] Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).<ref>PMID:18620547</ref> | ||
==See Also== | ==See Also== | ||
Line 15: | Line 16: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Church | [[Category: Church WB]] | ||
[[Category: Jayawickrama | [[Category: Jayawickrama GS]] | ||
[[Category: Nematollahi | [[Category: Nematollahi A]] | ||
[[Category: Sun | [[Category: Sun G]] | ||
Latest revision as of 18:14, 4 October 2023
Crystal structure of Kynurenine Aminotransferase-II in apo-form, at 1.47 A resolutionCrystal structure of Kynurenine Aminotransferase-II in apo-form, at 1.47 A resolution
Structural highlights
FunctionAADAT_HUMAN Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).[1] See AlsoReferences
|
|